ArticleChemical science2019
The biosynthetic implications of late-stage condensation domain selectivity during glycopeptide antibiotic biosynthesis.
Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Structure, Function and Engineering of the Nonribosomal Peptide Synthetase Condensation Domain.International journal of molecular sciences · 2024Review
- High-throughput reprogramming of an NRPS condensation domain.Nature chemical biology · 2024Article
- Controlling Substrate- and Stereospecificity of Condensation Domains in Nonribosomal Peptide Synthetases.ACS chemical biology · 2024Article
- Probing Substrate-Loaded Carrier Proteins by Nuclear Magnetic Resonance.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Global protein dynamics as communication sensors in peptide synthetase domains.Science advances · 2022Article
- Evolutionary and functional analysis of an NRPS condensation domain integrates β-lactam, ᴅ-amino acid, and dehydroamino acid synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Exploring modular reengineering strategies to redesign the teicoplanin non-ribosomal peptide synthetase.Chemical science · 2020Article
- Teicoplanin biosynthesis: unraveling the interplay of structural, regulatory, and resistance genes.Applied microbiology and biotechnology · 2020Review
- New Molecular Tools for Regulation and Improvement of A40926 Glycopeptide Antibiotic Production inFrontiers in microbiology · 2020Article
- Biological, chemical, and biochemical strategies for modifying glycopeptide antibiotics.The Journal of biological chemistry · 2019Review
- A proof-reading mechanism for non-proteinogenic amino acid incorporation into glycopeptide antibiotics.Chemical science · 2019Article
- Kistamicin biosynthesis reveals the biosynthetic requirements for production of highly crosslinked glycopeptide antibiotics.Nature communications · 2019Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Non-ribosomal peptide synthesis is a highly important biosynthetic pathway for the formation of many secondary metabolites of medical relevance. Due to the challenges associated with the chemical synthesis of many of the products of these assembly lines, understanding the activity and selectivity of non-ribosomal peptide synthetase (NRPS) machineries is an essential step towards the redesign of such machineries to produce new bioactive peptides. Whilst the selectivity of the adenylation domains responsible for amino acid activation during NRPS synthesis has been widely studied, the selectivity of the essential peptide bond forming domains - known as condensation domains - is not well understood. Here, we present the results of a combination of
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.